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P20020

- AT2B1_HUMAN

UniProt

P20020 - AT2B1_HUMAN

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Protein

Plasma membrane calcium-transporting ATPase 1

Gene

ATP2B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell.

Catalytic activityi

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei475 – 47514-aspartylphosphate intermediate
Metal bindingi797 – 7971MagnesiumBy similarity
Metal bindingi801 – 8011MagnesiumBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium-transporting ATPase activity Source: ProtInc
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. ion transmembrane transport Source: Reactome
  3. transmembrane transport Source: Reactome
  4. transport Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Calmodulin-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_23765. Reduction of cytosolic Ca++ levels.
REACT_25149. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.2.25. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Plasma membrane calcium-transporting ATPase 1 (EC:3.6.3.8)
Short name:
PMCA1
Alternative name(s):
Plasma membrane calcium ATPase isoform 1
Plasma membrane calcium pump isoform 1
Gene namesi
Name:ATP2B1
Synonyms:PMCA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:814. ATP2B1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. integral component of plasma membrane Source: ProtInc
  3. membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25107.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12581257Plasma membrane calcium-transporting ATPase 1PRO_0000046209Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine1 Publication
Modified residuei17 – 171Phosphoserine1 Publication
Modified residuei1116 – 11161Phosphothreonine; by PKC
Modified residuei1193 – 11931Phosphoserine4 Publications
Modified residuei1203 – 12031Phosphothreonine2 Publications
Modified residuei1216 – 12161Phosphoserine; by PKA2 Publications
Modified residuei1220 – 12201Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP20020.
PaxDbiP20020.
PRIDEiP20020.

PTM databases

PhosphoSiteiP20020.

Expressioni

Tissue specificityi

Isoform B is ubiquitously expressed. Isoform C is found in brain cortex, skeletal muscle and heart muscle. Isoform D has only been found in fetal skeletal muscle. Isoform K has been found in small intestine and liver.

Gene expression databases

BgeeiP20020.
CleanExiHS_ATP2B1.
ExpressionAtlasiP20020. baseline and differential.
GenevestigatoriP20020.

Organism-specific databases

HPAiCAB005605.
HPA011166.
HPA012945.

Interactioni

Subunit structurei

Interacts with PDZD11. Interacts with SLC35G1 and STIM1.2 Publications

Protein-protein interaction databases

BioGridi106980. 10 interactions.
IntActiP20020. 5 interactions.
MINTiMINT-5004114.
STRINGi9606.ENSP00000261173.

Structurei

3D structure databases

ProteinModelPortaliP20020.
SMRiP20020. Positions 66-946, 1100-1126.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 9796CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini119 – 15436ExtracellularSequence AnalysisAdd
BLAST
Topological domaini176 – 366191CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini387 – 41933ExtracellularSequence AnalysisAdd
BLAST
Topological domaini438 – 852415CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini873 – 88210ExtracellularSequence Analysis
Topological domaini904 – 92320CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini947 – 96418ExtracellularSequence AnalysisAdd
BLAST
Topological domaini987 – 100519CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1028 – 103710ExtracellularSequence Analysis
Topological domaini1060 – 1258199CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei98 – 11821HelicalSequence AnalysisAdd
BLAST
Transmembranei155 – 17521HelicalSequence AnalysisAdd
BLAST
Transmembranei367 – 38620HelicalSequence AnalysisAdd
BLAST
Transmembranei420 – 43718HelicalSequence AnalysisAdd
BLAST
Transmembranei853 – 87220HelicalSequence AnalysisAdd
BLAST
Transmembranei883 – 90321HelicalSequence AnalysisAdd
BLAST
Transmembranei924 – 94623HelicalSequence AnalysisAdd
BLAST
Transmembranei965 – 98622HelicalSequence AnalysisAdd
BLAST
Transmembranei1006 – 102722HelicalSequence AnalysisAdd
BLAST
Transmembranei1038 – 105922HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1100 – 111718Calmodulin-binding subdomain AAdd
BLAST
Regioni1118 – 112710Calmodulin-binding subdomain B

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi296 – 2994Poly-Glu

Domaini

The calmodulin-binding subdomain B is different in the different splice variants and shows pH dependent calmodulin binding properties in isoforms A, C, D and E.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00510000046331.
HOVERGENiHBG061286.
InParanoidiP20020.
KOiK05850.
OMAiNNSVAYG.
OrthoDBiEOG7SN8BN.
PhylomeDBiP20020.
TreeFamiTF300330.

Family and domain databases

Gene3Di1.20.1110.10. 1 hit.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR022141. ATP_Ca_trans_C.
IPR006408. ATPase_P-typ_Ca-transp_plasma.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF12424. ATP_Ca_trans_C. 2 hits.
PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform D (identifier: P20020-1) [UniParc]FASTAAdd to Basket

Also known as: CIV

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGDMANNSVA YSGVKNSLKE ANHDGDFGIT LAELRALMEL RSTDALRKIQ
60 70 80 90 100
ESYGDVYGIC TKLKTSPNEG LSGNPADLER REAVFGKNFI PPKKPKTFLQ
110 120 130 140 150
LVWEALQDVT LIILEIAAIV SLGLSFYQPP EGDNALCGEV SVGEEEGEGE
160 170 180 190 200
TGWIEGAAIL LSVVCVVLVT AFNDWSKEKQ FRGLQSRIEQ EQKFTVIRGG
210 220 230 240 250
QVIQIPVADI TVGDIAQVKY GDLLPADGIL IQGNDLKIDE SSLTGESDHV
260 270 280 290 300
KKSLDKDPLL LSGTHVMEGS GRMVVTAVGV NSQTGIIFTL LGAGGEEEEK
310 320 330 340 350
KDEKKKEKKN KKQDGAIENR NKAKAQDGAA MEMQPLKSEE GGDGDEKDKK
360 370 380 390 400
KANLPKKEKS VLQGKLTKLA VQIGKAGLLM SAITVIILVL YFVIDTFWVQ
410 420 430 440 450
KRPWLAECTP IYIQYFVKFF IIGVTVLVVA VPEGLPLAVT ISLAYSVKKM
460 470 480 490 500
MKDNNLVRHL DACETMGNAT AICSDKTGTL TMNRMTVVQA YINEKHYKKV
510 520 530 540 550
PEPEAIPPNI LSYLVTGISV NCAYTSKILP PEKEGGLPRH VGNKTECALL
560 570 580 590 600
GLLLDLKRDY QDVRNEIPEE ALYKVYTFNS VRKSMSTVLK NSDGSYRIFS
610 620 630 640 650
KGASEIILKK CFKILSANGE AKVFRPRDRD DIVKTVIEPM ASEGLRTICL
660 670 680 690 700
AFRDFPAGEP EPEWDNENDI VTGLTCIAVV GIEDPVRPEV PDAIKKCQRA
710 720 730 740 750
GITVRMVTGD NINTARAIAT KCGILHPGED FLCLEGKDFN RRIRNEKGEI
760 770 780 790 800
EQERIDKIWP KLRVLARSSP TDKHTLVKGI IDSTVSDQRQ VVAVTGDGTN
810 820 830 840 850
DGPALKKADV GFAMGIAGTD VAKEASDIIL TDDNFTSIVK AVMWGRNVYD
860 870 880 890 900
SISKFLQFQL TVNVVAVIVA FTGACITQDS PLKAVQMLWV NLIMDTLASL
910 920 930 940 950
ALATEPPTES LLLRKPYGRN KPLISRTMMK NILGHAFYQL VVVFTLLFAG
960 970 980 990 1000
EKFFDIDSGR NAPLHAPPSE HYTIVFNTFV LMQLFNEINA RKIHGERNVF
1010 1020 1030 1040 1050
EGIFNNAIFC TIVLGTFVVQ IIIVQFGGKP FSCSELSIEQ WLWSIFLGMG
1060 1070 1080 1090 1100
TLLWGQLIST IPTSRLKFLK EAGHGTQKEE IPEEELAEDV EEIDHAEREL
1110 1120 1130 1140 1150
RRGQILWFRG LNRIQTQMDV VNAFQSGSSI QGALRRQPSI ASQHHDVTNI
1160 1170 1180 1190 1200
STPTHIRVVN AFRSSLYEGL EKPESRSSIH NFMTHPEFRI EDSEPHIPLI
1210 1220 1230 1240 1250
DDTDAEDDAP TKRNSSPPPS PNKNNNAVDS GIHLTIEMNK SATSSSPGSP

LHSLETSL
Length:1,258
Mass (Da):138,755
Last modified:June 1, 2001 - v3
Checksum:i7037112747FC9B0A
GO
Isoform A (identifier: P20020-2) [UniParc]FASTAAdd to Basket

Also known as: CII

The sequence of this isoform differs from the canonical sequence as follows:
     1156-1258: IRVVNAFRSS...SPLHSLETSL → VVFSSSTASTTVGYSSGECIS

Show »
Length:1,176
Mass (Da):129,516
Checksum:i5672202C16491703
GO
Isoform B (identifier: P20020-3) [UniParc]FASTAAdd to Basket

Also known as: CI

The sequence of this isoform differs from the canonical sequence as follows:
     1118-1155: Missing.

Show »
Length:1,220
Mass (Da):134,685
Checksum:i7E75C19B1A501423
GO
Isoform C (identifier: P20020-4) [UniParc]FASTAAdd to Basket

Also known as: CIII

The sequence of this isoform differs from the canonical sequence as follows:
     1147-1155: Missing.

Show »
Length:1,249
Mass (Da):137,804
Checksum:i8F56F132BE096587
GO
Isoform E (identifier: P20020-5) [UniParc]FASTAAdd to Basket

Also known as: CV

The sequence of this isoform differs from the canonical sequence as follows:
     1156-1258: IRVVNAFRSS...SPLHSLETSL → VVFSSSTASTTVGFEW

Show »
Length:1,171
Mass (Da):129,152
Checksum:i9FC9B1AA3B32B384
GO
Isoform K (identifier: P20020-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1021-1056: Missing.
     1118-1155: Missing.

Show »
Length:1,184
Mass (Da):130,617
Checksum:iB1FB3E7116D2FDA2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2624LLLS → MSAT in AAA36000. (PubMed:8386431)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti267 – 2671M → R Rare polymorphism. 1 Publication
VAR_000698

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1021 – 105636Missing in isoform K. CuratedVSP_000372Add
BLAST
Alternative sequencei1118 – 115538Missing in isoform B and isoform K. 2 PublicationsVSP_000373Add
BLAST
Alternative sequencei1147 – 11559Missing in isoform C. CuratedVSP_000374
Alternative sequencei1156 – 1258103IRVVN…LETSL → VVFSSSTASTTVGYSSGECI S in isoform A. CuratedVSP_000375Add
BLAST
Alternative sequencei1156 – 1258103IRVVN…LETSL → VVFSSSTASTTVGFEW in isoform E. CuratedVSP_000376Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04027 mRNA. Translation: AAA74511.1.
M95541 mRNA. Translation: AAA35999.1.
M95542 mRNA. Translation: AAA36000.1.
L14561 Genomic DNA. Translation: AAD09924.1.
L14561 Genomic DNA. Translation: AAD09925.1.
M25824 Genomic DNA. Translation: AAA58383.1.
M25824 Genomic DNA. Translation: AAA58382.1.
M25824 Genomic DNA. Translation: AAA58381.1.
S49852 mRNA. Translation: AAB24324.1.
U15686 mRNA. Translation: AAA60983.1.
U15687 mRNA. Translation: AAA60984.1.
CCDSiCCDS41817.1. [P20020-2]
CCDS9035.1. [P20020-3]
PIRiA30802.
E49570.
I55491.
I70165.
RefSeqiNP_001001323.1. NM_001001323.1. [P20020-2]
NP_001673.2. NM_001682.2. [P20020-3]
XP_005268976.1. XM_005268919.1. [P20020-4]
UniGeneiHs.506276.

Genome annotation databases

EnsembliENST00000261173; ENSP00000261173; ENSG00000070961. [P20020-3]
ENST00000359142; ENSP00000352054; ENSG00000070961. [P20020-2]
ENST00000428670; ENSP00000392043; ENSG00000070961. [P20020-3]
GeneIDi490.
KEGGihsa:490.
UCSCiuc001tbf.3. human. [P20020-6]
uc001tbg.3. human. [P20020-2]
uc001tbh.3. human. [P20020-3]

Polymorphism databases

DMDMi14286104.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04027 mRNA. Translation: AAA74511.1 .
M95541 mRNA. Translation: AAA35999.1 .
M95542 mRNA. Translation: AAA36000.1 .
L14561 Genomic DNA. Translation: AAD09924.1 .
L14561 Genomic DNA. Translation: AAD09925.1 .
M25824 Genomic DNA. Translation: AAA58383.1 .
M25824 Genomic DNA. Translation: AAA58382.1 .
M25824 Genomic DNA. Translation: AAA58381.1 .
S49852 mRNA. Translation: AAB24324.1 .
U15686 mRNA. Translation: AAA60983.1 .
U15687 mRNA. Translation: AAA60984.1 .
CCDSi CCDS41817.1. [P20020-2 ]
CCDS9035.1. [P20020-3 ]
PIRi A30802.
E49570.
I55491.
I70165.
RefSeqi NP_001001323.1. NM_001001323.1. [P20020-2 ]
NP_001673.2. NM_001682.2. [P20020-3 ]
XP_005268976.1. XM_005268919.1. [P20020-4 ]
UniGenei Hs.506276.

3D structure databases

ProteinModelPortali P20020.
SMRi P20020. Positions 66-946, 1100-1126.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106980. 10 interactions.
IntActi P20020. 5 interactions.
MINTi MINT-5004114.
STRINGi 9606.ENSP00000261173.

Protein family/group databases

TCDBi 3.A.3.2.25. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSitei P20020.

Polymorphism databases

DMDMi 14286104.

Proteomic databases

MaxQBi P20020.
PaxDbi P20020.
PRIDEi P20020.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261173 ; ENSP00000261173 ; ENSG00000070961 . [P20020-3 ]
ENST00000359142 ; ENSP00000352054 ; ENSG00000070961 . [P20020-2 ]
ENST00000428670 ; ENSP00000392043 ; ENSG00000070961 . [P20020-3 ]
GeneIDi 490.
KEGGi hsa:490.
UCSCi uc001tbf.3. human. [P20020-6 ]
uc001tbg.3. human. [P20020-2 ]
uc001tbh.3. human. [P20020-3 ]

Organism-specific databases

CTDi 490.
GeneCardsi GC12M089981.
HGNCi HGNC:814. ATP2B1.
HPAi CAB005605.
HPA011166.
HPA012945.
MIMi 108731. gene.
neXtProti NX_P20020.
PharmGKBi PA25107.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0474.
GeneTreei ENSGT00510000046331.
HOVERGENi HBG061286.
InParanoidi P20020.
KOi K05850.
OMAi NNSVAYG.
OrthoDBi EOG7SN8BN.
PhylomeDBi P20020.
TreeFami TF300330.

Enzyme and pathway databases

Reactomei REACT_23765. Reduction of cytosolic Ca++ levels.
REACT_25149. Ion transport by P-type ATPases.

Miscellaneous databases

GeneWikii ATP2B1.
GenomeRNAii 490.
NextBioi 2053.
PROi P20020.
SOURCEi Search...

Gene expression databases

Bgeei P20020.
CleanExi HS_ATP2B1.
ExpressionAtlasi P20020. baseline and differential.
Genevestigatori P20020.

Family and domain databases

Gene3Di 1.20.1110.10. 1 hit.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProi IPR022141. ATP_Ca_trans_C.
IPR006408. ATPase_P-typ_Ca-transp_plasma.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view ]
Pfami PF12424. ATP_Ca_trans_C. 2 hits.
PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
SMARTi SM00831. Cation_ATPase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsi TIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete primary structure of a human plasma membrane Ca2+ pump."
    Verma A.K., Filoteo A.G., Stanford D.R., Wieben E.D., Penniston J.T., Strehler E.E., Fischer R., Heim R., Vogel G., Mathews S., Strehler-Page M.-A., James P., Vorherr T.E., Krebs J., Carafoli E.
    J. Biol. Chem. 263:14152-14159(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    Tissue: Erythrocyte.
  2. "Molecular cloning of a plasma membrane calcium pump from human osteoblasts."
    Kumar R., Haugen J.D., Penniston J.T.
    J. Bone Miner. Res. 8:505-513(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    Tissue: Osteoblast.
  3. "Structure of the gene encoding the human plasma membrane calcium pump isoform 1."
    Hilfiker H., Strehler-Page M.-A., Stauffer T.P., Carafoli E., Strehler E.E.
    J. Biol. Chem. 268:19717-19725(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
    Tissue: Leukocyte.
  4. Strehler E.E., Strehler-Page M.-A.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  5. "mRNAs for plasma membrane calcium pump isoforms differing in their regulatory domain are generated by alternative splicing that involves two internal donor sites in a single exon."
    Strehler E.E., Strehler-Page M.-A., Vogel G., Carafoli E.
    Proc. Natl. Acad. Sci. U.S.A. 86:6908-6912(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A; C AND D).
    Tissue: Fetal skeletal muscle.
  6. "Study of calmodulin binding to the alternatively spliced C-terminal domain of the plasma membrane Ca2+ pump."
    Kessler F., Falchetto R., Heim R., Meili R., Vorherr T.E., Strehler E.E., Carafoli E.
    Biochemistry 31:11785-11792(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    Tissue: Fetal brain.
  7. "Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes."
    Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.
    J. Biol. Chem. 268:25993-26003(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND E).
    Tissue: Brain cortex.
  8. Erratum
    Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.
    J. Biol. Chem. 269:32022-32022(1994) [PubMed] [Europe PMC] [Abstract]
  9. "Human and rat intestinal plasma membrane calcium pump isoforms."
    Howard A., Legon S., Walters J.R.
    Am. J. Physiol. 265:G917-G925(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM K).
    Tissue: Small intestine mucosa.
  10. "Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump."
    James P.H., Pruschy M., Vorherr T.E., Penniston J.T., Carafoli E.
    Biochemistry 28:4253-4258(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CAMP KINASE.
  11. "Protein kinase C phosphorylates the carboxyl terminus of the plasma membrane Ca(2+)-ATPase from human erythrocytes."
    Wang K.K.W., Wright L.C., Machan C.L., Allen B.G., Conigrave A.D., Roufogalis B.D.
    J. Biol. Chem. 266:9078-9085(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PROTEIN KINASE C.
  12. "Characterization of PISP, a novel single-PDZ protein that binds to all plasma membrane Ca2+-ATPase b-splice variants."
    Goellner G.M., DeMarco S.J., Strehler E.E.
    Ann. N. Y. Acad. Sci. 986:461-471(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDZD11.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1193 AND SER-1220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-1193; THR-1203; SER-1216 AND SER-1220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1193 AND THR-1203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to multiple transporters."
    Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.
    Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC35G1 AND STIM1.
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1193; SER-1216 AND SER-1220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Investigation of the Met-267 Arg exchange in isoform 1 of the human plasma membrane calcium pump in patients with essential hypertension by the amplification-created restriction site technique."
    Benkwitz C., Kubsisch C., Kraft K., Neyses L.
    J. Mol. Med. 75:62-66(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-267.

Entry informationi

Entry nameiAT2B1_HUMAN
AccessioniPrimary (citable) accession number: P20020
Secondary accession number(s): Q12992
, Q12993, Q13819, Q13820, Q13821, Q16504, Q93082
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3